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Unfolding the Mysteries of Protein Metamorphosis. ACS Chem Biol 2018 Jun 15;13(6):1438-1446



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Scopus ID

2-s2.0-85047568358 (requires institutional sign-in at Scopus site)   61 Citations


Since the proposal of Anfinsen's thermodynamic hypothesis in 1963, our understanding of protein folding and dynamics has gained significant appreciation of its nuance and complexity. Intrinsically disordered proteins, chameleonic sequences, morpheeins, and metamorphic proteins have broadened the protein folding paradigm. Here, we discuss noncanonical protein folding patterns, with an emphasis on metamorphic proteins, and we review known metamorphic proteins that occur naturally and that have been engineered in the laboratory. Finally, we discuss research areas surrounding metamorphic proteins that are primed for future exploration, including evolution, drug discovery, and the quest for previously unrecognized metamorphs. As we enter an age where we are capable of complex bioinformatic searches and de novo protein design, we are primed to search for previously unrecognized metamorphic proteins and to design our own metamorphs to act as targeted, switchable drugs; biosensors; and more.

Author List

Dishman AF, Volkman BF


Acacia Frances Dishman MD, PhD Postdoctoral Fellow in the Biochemistry department at Medical College of Wisconsin
Brian F. Volkman PhD Professor in the Biochemistry department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Intrinsically Disordered Proteins
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Engineering
Protein Folding
Protein Unfolding